Chemical relaxation studies of metal ion activated enzymes. I. Opposing bicipital relaxation phenomena in the bovine carbonic anhydrase system. Theory and observation

1975 ◽  
Vol 97 (1) ◽  
pp. 173-177 ◽  
Author(s):  
Dennis E. Tallman ◽  
George Graf ◽  
Timothy J. McNeese ◽  
Mark M. Wilson
Keyword(s):  
System Theory ◽  
Carbonic Anhydrase ◽  
Metal Ion ◽  
Relaxation Phenomena ◽  
Bovine Carbonic Anhydrase ◽  
Chemical Relaxation ◽  
Relaxation Studies

Characterization of cobalt(II) bovine carbonic anhydrase and of its derivatives

1978 ◽  
Vol 100 (15) ◽  
pp. 4873-4877 ◽  
Author(s):  
I. Bertini ◽  
G. Canti ◽  
C. Luchinat ◽  
A. Scozzafava
Keyword(s):  
Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase

scholarly journals Protein Folding by Domain V of Escherichia coli 23S rRNA: Specificity of RNA-Protein Interactions

2008 ◽  
Vol 190 (9) ◽  
pp. 3344-3352 ◽  
Author(s):  
Dibyendu Samanta ◽  
Debashis Mukhopadhyay ◽  
Saheli Chowdhury ◽  
Jaydip Ghosh ◽  
Saumen Pal ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Folding ◽  
Carbonic Anhydrase ◽  
Protein Interactions ◽  
23S Rrna ◽  
Unfolded Proteins ◽  
Bovine Carbonic Anhydrase ◽  
Egg White Lysozyme ◽  
General Protein ◽  
Domain V

ABSTRACT The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.

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